Research workbench
Structure of antigen-Fab complex with engineered switch residue region.
Analyse Structure of antigen-Fab complex with engineered switch residue region. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5UCB
- Type
- protein
- Length
- 580 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fab heavy chain; Fab light chain; Histone chaperone ASF1
- UniProt
- P32447
- Pockets
- 6 · best druggability 0.60
Structure
x-ray diffraction · 3 distinct chains · 8% helix, 53% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| H | Fab heavy chain | protein | 217 | 7% helix, 53% strand | — |
| L | Fab light chain | protein | 210 | 8% helix, 52% strand | — |
| B | Histone chaperone ASF1 | protein | 153 | 10% helix, 54% strand | P32447 |
Pockets
6 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 477 | 0.60 | 0.75 | 61 | empty |
| 2 | 59 | 0.46 | 0.84 | 22 | empty |
| 3 | 102 | 0.39 | 0.76 | 27 | empty |
| 4 | 105 | 0.37 | 0.74 | 22 | empty |
| 5 | 62 | 0.33 | 0.77 | 19 | empty |
Interfaces
3 interfaces between chains.
- H–L · 1954 Ų buried · 13 hydrogen bonds · protein-protein
- H–B · 805 Ų buried · 8 hydrogen bonds · protein-protein
- L–B · 619 Ų buried · 15 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 disulfide (disulfide).
Compared structures
- 5UCB · Structure of antigen-Fab complex with engineered switch residue region. · the same entry in another collection · chain L against L, TM-score 1.00
- P32447 · AlphaFold monomer V2.0 prediction for histone chaperone ASF1 (P32447) · a predicted model of the same protein · chain B against A, TM-score 0.95
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P32447
- Elsewhere: RCSB PDB 5UCB · PDBe 5UCB · UniProt P32447
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